DK147812B - Fremgangsmaade til fremstilling af et stabilt lyofiliseret urokinasepraeparat - Google Patents

Fremgangsmaade til fremstilling af et stabilt lyofiliseret urokinasepraeparat Download PDF

Info

Publication number: DK147812B
Authority: DK; Denmark
Prior art keywords: urokinase; hsa; lyophilized; amino acid; preparation
Prior art date: 1978-05-12

Application number

DK195079AA

Other languages

Danish (da)

English (en)

Other versions

DK195079A (da

Inventor

Yoshiya Yamahira

Keiji Fujioka

Yoshiko Okuzawa

Seiko Miura

Shigeji Sato

Original Assignee

Sumitomo Chemical Co

Priority date (The priority date is an assumption and is not a legal conclusion. Google has not performed a legal analysis and makes no representation as to the accuracy of the date listed.)

1978-05-12

Filing date

1979-05-10

Publication date

1984-12-17

1979-05-10 Application filed by Sumitomo Chemical Co filed Critical Sumitomo Chemical Co

1979-11-13 Publication of DK195079A publication Critical patent/DK195079A/da

1984-12-17 Publication of DK147812B publication Critical patent/DK147812B/da

Links

102000003990 Urokinase-type plasminogen activator Human genes 0.000 title description 68
108090000435 Urokinase-type plasminogen activator Proteins 0.000 title description 68
229960005356 urokinase Drugs 0.000 title description 68
238000002360 preparation method Methods 0.000 title description 24
238000000034 method Methods 0.000 title description 12
235000001014 amino acid Nutrition 0.000 description 30
229940024606 amino acid Drugs 0.000 description 30
WHUUTDBJXJRKMK-UHFFFAOYSA-N Glutamic acid Natural products OC(=O)C(N)CCC(O)=O WHUUTDBJXJRKMK-UHFFFAOYSA-N 0.000 description 23
150000001413 amino acids Chemical class 0.000 description 20
235000013922 glutamic acid Nutrition 0.000 description 16
239000004220 glutamic acid Substances 0.000 description 16
239000000243 solution Substances 0.000 description 16
AYFVYJQAPQTCCC-GBXIJSLDSA-N L-threonine Chemical compound C[C@@H](O)[C@H](N)C(O)=O AYFVYJQAPQTCCC-GBXIJSLDSA-N 0.000 description 12
239000003381 stabilizer Substances 0.000 description 11
-1 amino acid compounds Chemical class 0.000 description 10
239000007924 injection Substances 0.000 description 10
238000002347 injection Methods 0.000 description 10
230000000087 stabilizing effect Effects 0.000 description 10
230000002537 thrombolytic effect Effects 0.000 description 10
AYFVYJQAPQTCCC-UHFFFAOYSA-N Threonine Natural products CC(O)C(N)C(O)=O AYFVYJQAPQTCCC-UHFFFAOYSA-N 0.000 description 8
239000004473 Threonine Substances 0.000 description 8
230000000694 effects Effects 0.000 description 8
239000000203 mixture Substances 0.000 description 7
239000008055 phosphate buffer solution Substances 0.000 description 7
150000003839 salts Chemical class 0.000 description 7
239000007864 aqueous solution Substances 0.000 description 6
238000002474 experimental method Methods 0.000 description 5
FBPFZTCFMRRESA-KVTDHHQDSA-N D-Mannitol Chemical compound OC[C@@H](O)[C@@H](O)[C@H](O)[C@H](O)CO FBPFZTCFMRRESA-KVTDHHQDSA-N 0.000 description 4
229930195725 Mannitol Natural products 0.000 description 4
239000000594 mannitol Substances 0.000 description 4
235000010355 mannitol Nutrition 0.000 description 4
239000011734 sodium Substances 0.000 description 4
102000004190 Enzymes Human genes 0.000 description 3
108090000790 Enzymes Proteins 0.000 description 3
239000002253 acid Substances 0.000 description 3
MSWZFWKMSRAUBD-UHFFFAOYSA-N beta-D-galactosamine Natural products NC1C(O)OC(CO)C(O)C1O MSWZFWKMSRAUBD-UHFFFAOYSA-N 0.000 description 3
MSWZFWKMSRAUBD-QZABAPFNSA-N beta-D-glucosamine Chemical compound N[C@H]1[C@H](O)O[C@H](CO)[C@@H](O)[C@@H]1O MSWZFWKMSRAUBD-QZABAPFNSA-N 0.000 description 3
229940088598 enzyme Drugs 0.000 description 3
239000003527 fibrinolytic agent Substances 0.000 description 3
102000009027 Albumins Human genes 0.000 description 2
108010088751 Albumins Proteins 0.000 description 2
102000008100 Human Serum Albumin Human genes 0.000 description 2
108091006905 Human Serum Albumin Proteins 0.000 description 2
XUJNEKJLAYXESH-REOHCLBHSA-N L-Cysteine Chemical compound SC[C@H](N)C(O)=O XUJNEKJLAYXESH-REOHCLBHSA-N 0.000 description 2
239000002671 adjuvant Substances 0.000 description 2
210000004369 blood Anatomy 0.000 description 2
239000008280 blood Substances 0.000 description 2
PXEDJBXQKAGXNJ-QTNFYWBSSA-L disodium L-glutamate Chemical compound [Na+].[Na+].[O-]C(=O)[C@@H](N)CCC([O-])=O PXEDJBXQKAGXNJ-QTNFYWBSSA-L 0.000 description 2
230000003480 fibrinolytic effect Effects 0.000 description 2
238000004108 freeze drying Methods 0.000 description 2
HNDVDQJCIGZPNO-UHFFFAOYSA-N histidine Natural products OC(=O)C(N)CC1=CN=CN1 HNDVDQJCIGZPNO-UHFFFAOYSA-N 0.000 description 2
238000001727 in vivo Methods 0.000 description 2
235000013923 monosodium glutamate Nutrition 0.000 description 2
125000002924 primary amino group Chemical group [H]N([H])* 0.000 description 2
238000000746 purification Methods 0.000 description 2
229940073490 sodium glutamate Drugs 0.000 description 2
230000002195 synergetic effect Effects 0.000 description 2
210000002700 urine Anatomy 0.000 description 2
LDXJRKWFNNFDSA-UHFFFAOYSA-N 2-(2,4,6,7-tetrahydrotriazolo[4,5-c]pyridin-5-yl)-1-[4-[2-[[3-(trifluoromethoxy)phenyl]methylamino]pyrimidin-5-yl]piperazin-1-yl]ethanone Chemical compound C1CN(CC2=NNN=C21)CC(=O)N3CCN(CC3)C4=CN=C(N=C4)NCC5=CC(=CC=C5)OC(F)(F)F LDXJRKWFNNFDSA-UHFFFAOYSA-N 0.000 description 1
239000004475 Arginine Substances 0.000 description 1
ODKSFYDXXFIFQN-BYPYZUCNSA-P L-argininium(2+) Chemical compound NC(=[NH2+])NCCC[C@H]([NH3+])C(O)=O ODKSFYDXXFIFQN-BYPYZUCNSA-P 0.000 description 1
HNDVDQJCIGZPNO-YFKPBYRVSA-N L-histidine Chemical compound OC(=O)[C@@H](N)CC1=CN=CN1 HNDVDQJCIGZPNO-YFKPBYRVSA-N 0.000 description 1
ROHFNLRQFUQHCH-YFKPBYRVSA-N L-leucine Chemical compound CC(C)C[C@H](N)C(O)=O ROHFNLRQFUQHCH-YFKPBYRVSA-N 0.000 description 1
FFEARJCKVFRZRR-BYPYZUCNSA-N L-methionine Chemical compound CSCC[C@H](N)C(O)=O FFEARJCKVFRZRR-BYPYZUCNSA-N 0.000 description 1
ROHFNLRQFUQHCH-UHFFFAOYSA-N Leucine Natural products CC(C)CC(N)C(O)=O ROHFNLRQFUQHCH-UHFFFAOYSA-N 0.000 description 1
241000283973 Oryctolagus cuniculus Species 0.000 description 1
108091000080 Phosphotransferase Proteins 0.000 description 1
239000000654 additive Substances 0.000 description 1
ODKSFYDXXFIFQN-UHFFFAOYSA-N arginine Natural products OC(=O)C(N)CCCNC(N)=N ODKSFYDXXFIFQN-UHFFFAOYSA-N 0.000 description 1
230000001580 bacterial effect Effects 0.000 description 1
239000003093 cationic surfactant Substances 0.000 description 1
230000000052 comparative effect Effects 0.000 description 1
235000018417 cysteine Nutrition 0.000 description 1
XUJNEKJLAYXESH-UHFFFAOYSA-N cysteine Natural products SCC(N)C(O)=O XUJNEKJLAYXESH-UHFFFAOYSA-N 0.000 description 1
230000003247 decreasing effect Effects 0.000 description 1
238000001514 detection method Methods 0.000 description 1
238000007865 diluting Methods 0.000 description 1
230000002255 enzymatic effect Effects 0.000 description 1
230000020764 fibrinolysis Effects 0.000 description 1
238000001914 filtration Methods 0.000 description 1
230000002209 hydrophobic effect Effects 0.000 description 1
238000000338 in vitro Methods 0.000 description 1
238000002955 isolation Methods 0.000 description 1
229930182817 methionine Natural products 0.000 description 1
102000020233 phosphotransferase Human genes 0.000 description 1
239000002504 physiological saline solution Substances 0.000 description 1
230000003389 potentiating effect Effects 0.000 description 1
230000001105 regulatory effect Effects 0.000 description 1
159000000000 sodium salts Chemical class 0.000 description 1
239000000126 substance Substances 0.000 description 1
230000001732 thrombotic effect Effects 0.000 description 1

Classifications

- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12N—MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
- C12N9/00—Enzymes; Proenzymes; Compositions thereof; Processes for preparing, activating, inhibiting, separating or purifying enzymes
- C12N9/14—Hydrolases (3)
- C12N9/48—Hydrolases (3) acting on peptide bonds (3.4)
- C12N9/50—Proteinases, e.g. Endopeptidases (3.4.21-3.4.25)
- C12N9/64—Proteinases, e.g. Endopeptidases (3.4.21-3.4.25) derived from animal tissue
- C12N9/6421—Proteinases, e.g. Endopeptidases (3.4.21-3.4.25) derived from animal tissue from mammals
- C12N9/6424—Serine endopeptidases (3.4.21)
- C12N9/6456—Plasminogen activators
- C12N9/6462—Plasminogen activators u-Plasminogen activator (3.4.21.73), i.e. urokinase
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K47/00—Medicinal preparations characterised by the non-active ingredients used, e.g. carriers or inert additives; Targeting or modifying agents chemically bound to the active ingredient
- A61K47/06—Organic compounds, e.g. natural or synthetic hydrocarbons, polyolefins, mineral oil, petrolatum or ozokerite
- A61K47/16—Organic compounds, e.g. natural or synthetic hydrocarbons, polyolefins, mineral oil, petrolatum or ozokerite containing nitrogen, e.g. nitro-, nitroso-, azo-compounds, nitriles, cyanates
- A61K47/18—Amines; Amides; Ureas; Quaternary ammonium compounds; Amino acids; Oligopeptides having up to five amino acids
- A61K47/183—Amino acids, e.g. glycine, EDTA or aspartame
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K47/00—Medicinal preparations characterised by the non-active ingredients used, e.g. carriers or inert additives; Targeting or modifying agents chemically bound to the active ingredient
- A61K47/30—Macromolecular organic or inorganic compounds, e.g. inorganic polyphosphates
- A61K47/42—Proteins; Polypeptides; Degradation products thereof; Derivatives thereof, e.g. albumin, gelatin or zein
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K9/00—Medicinal preparations characterised by special physical form
- A61K9/0012—Galenical forms characterised by the site of application
- A61K9/0019—Injectable compositions; Intramuscular, intravenous, arterial, subcutaneous administration; Compositions to be administered through the skin in an invasive manner
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12N—MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
- C12N9/00—Enzymes; Proenzymes; Compositions thereof; Processes for preparing, activating, inhibiting, separating or purifying enzymes
- C12N9/96—Stabilising an enzyme by forming an adduct or a composition; Forming enzyme conjugates
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12Y—ENZYMES
- C12Y304/00—Hydrolases acting on peptide bonds, i.e. peptidases (3.4)
- C12Y304/21—Serine endopeptidases (3.4.21)
- C12Y304/21073—Serine endopeptidases (3.4.21) u-Plasminogen activator (3.4.21.73), i.e. urokinase

Landscapes

Health & Medical Sciences (AREA)
Chemical & Material Sciences (AREA)
Life Sciences & Earth Sciences (AREA)
Engineering & Computer Science (AREA)
Organic Chemistry (AREA)
General Health & Medical Sciences (AREA)
Wood Science & Technology (AREA)
Medicinal Chemistry (AREA)
Zoology (AREA)
Genetics & Genomics (AREA)
Bioinformatics & Cheminformatics (AREA)
Public Health (AREA)
Veterinary Medicine (AREA)
Biomedical Technology (AREA)
Biochemistry (AREA)
General Engineering & Computer Science (AREA)
Animal Behavior & Ethology (AREA)
Epidemiology (AREA)
Pharmacology & Pharmacy (AREA)
Biotechnology (AREA)
Microbiology (AREA)
Molecular Biology (AREA)
Proteomics, Peptides & Aminoacids (AREA)
Inorganic Chemistry (AREA)
Chemical Kinetics & Catalysis (AREA)
General Chemical & Material Sciences (AREA)
Oil, Petroleum & Natural Gas (AREA)
Dermatology (AREA)
Medicinal Preparation (AREA)
Medicines That Contain Protein Lipid Enzymes And Other Medicines (AREA)
Enzymes And Modification Thereof (AREA)
Medicines Containing Material From Animals Or Micro-Organisms (AREA)

DK195079AA 1978-05-12 1979-05-10 Fremgangsmaade til fremstilling af et stabilt lyofiliseret urokinasepraeparat DK147812B (da)

Applications Claiming Priority (2)

Application Number	Priority Date	Filing Date	Title
JP5682678		1978-05-12
JP5682678A JPS54147916A (en)	1978-05-12	1978-05-12	Preparation of urokinase injection

Publications (2)

Publication Number	Publication Date
DK195079A DK195079A (da)	1979-11-13
DK147812B true DK147812B (da)	1984-12-17

Family

ID=13038173

Family Applications (1)

Application Number	Title	Priority Date	Filing Date
DK195079AA DK147812B (da)	1978-05-12	1979-05-10	Fremgangsmaade til fremstilling af et stabilt lyofiliseret urokinasepraeparat

Country Status (10)

Country	Link
US (1)	US4244943A (de)
JP (1)	JPS54147916A (de)
CA (1)	CA1115206A (de)
CH (1)	CH641046A5 (de)
DE (1)	DE2917899A1 (de)
DK (1)	DK147812B (de)
FR (1)	FR2425245A1 (de)
GB (1)	GB2021412B (de)
IT (1)	IT7949032A0 (de)
SE (1)	SE7904118L (de)

Families Citing this family (22)

* Cited by examiner, † Cited by third party
Publication number	Priority date	Publication date	Assignee	Title
JPS5813521A (ja) *	1981-07-16	1983-01-26	Green Cross Corp:The	ミエロペルオキシダ−ゼの粉末製剤
US4350659A (en) *	1981-07-30	1982-09-21	Corning Glass Works	Stabilization of sensitive biologically active intermediate metabolites such as folic acid derivatives
JPS59139323A (ja) *	1983-01-28	1984-08-10	Green Cross Corp:The	ウロキナ−ゼ乾燥製剤
SU1128601A1 (ru) *	1983-05-10	1985-07-15	Всесоюзный кардиологический научный центр АМН СССР	Урокиназа,иммобилизированна на фибриногене
JPS6051119A (ja) *	1983-08-30	1985-03-22	Green Cross Corp:The	ウロキナ−ゼ乾燥製剤
JPS61111684A (ja) *	1984-11-05	1986-05-29	Terumo Corp	精製されたウロキナ−ゼ複合体の製造方法
JPS61124383A (ja) *	1984-11-16	1986-06-12	Unitika Ltd	固定化線維素溶解活性酵素の安定化法
WO1986003973A1 (fr) *	1985-01-14	1986-07-17	Terumo Kabushiki Kaisha	Complexe d'urokinase fibrinophile et procede de preparation
JPS61238732A (ja) *	1985-04-16	1986-10-24	Green Cross Corp:The	ウロキナーゼ前駆体乾燥製剤
KR940003056B1 (ko) *	1985-04-16	1994-04-13	가부시끼가이샤 미도리 쥬우지	우로키나제 전구체를 안정화시키는 방법
NZ217844A (en) *	1985-10-11	1989-10-27	Sumitomo Pharma	A sustained release pharmaceutical composition containing silicone elastomer and an albumin
JP2708749B2 (ja) *	1987-08-10	1998-02-04	エーザイ株式会社	修飾型ｔＰＡ含有注射用組成物
WO1990001334A1 (en) *	1988-08-05	1990-02-22	Codon	Formulations for plasminogen activator using aspartate
US4980165A (en) *	1989-01-27	1990-12-25	Genetics Institute, Inc.	Pharmaceutical formulations of plasminogen activator proteins
JPH02268681A (ja) *	1989-04-07	1990-11-02	Green Cross Corp:The	ウロキナーゼ前駆体の安定化方法及び乾燥製剤
WO1990014078A1 (en) *	1989-05-17	1990-11-29	Research Corporation Technologies, Inc.	Method and composition for the treatment of thrombosis in a mammal
EP0406008B1 (de) *	1989-06-30	1994-09-21	Ucar Carbon Technology Corporation	Graphitfolie
USD403943S (en)	1997-01-24	1999-01-12	Peter James Curry	Detachable hand grip tool
EP2236617A1 (de) *	2009-03-31	2010-10-06	Leukocare Ag	Verfahren zur Endsterilisierung von biofunktionalen Zusammensetzungen
RU2588658C2 (ru)	2010-04-27	2016-07-10	ЭсСиАйЭл Текнолоджи ГмбХ	Стабильные водные композиции белка mia/cd-rap
CN104906054B (zh) *	2015-06-15	2017-08-25	武汉人福药业有限责任公司	一种尿激酶冻干剂的制备方法
CN111450052A (zh) *	2020-04-22	2020-07-28	南京南大药业有限责任公司	一种尿激酶注射液制备方法

Family Cites Families (2)

* Cited by examiner, † Cited by third party
Publication number	Priority date	Publication date	Assignee	Title
BE665076A (de) *	1963-12-23	1965-12-08
JPS5137343B2 (de) *	1972-12-07	1976-10-15

1978
- 1978-05-12 JP JP5682678A patent/JPS54147916A/ja active Pending
1979
- 1979-05-03 DE DE19792917899 patent/DE2917899A1/de not_active Withdrawn
- 1979-05-09 US US06/037,280 patent/US4244943A/en not_active Expired - Lifetime
- 1979-05-10 CH CH438379A patent/CH641046A5/de not_active IP Right Cessation
- 1979-05-10 DK DK195079AA patent/DK147812B/da not_active Application Discontinuation
- 1979-05-10 FR FR7911841A patent/FR2425245A1/fr active Granted
- 1979-05-10 SE SE7904118A patent/SE7904118L/xx not_active Application Discontinuation
- 1979-05-10 GB GB7916251A patent/GB2021412B/en not_active Expired
- 1979-05-11 CA CA327,420A patent/CA1115206A/en not_active Expired
- 1979-05-11 IT IT7949032A patent/IT7949032A0/it unknown

Also Published As

Publication number	Publication date
DK195079A (da)	1979-11-13
IT7949032A0 (it)	1979-05-11
CH641046A5 (de)	1984-02-15
CA1115206A (en)	1981-12-29
JPS54147916A (en)	1979-11-19
GB2021412A (en)	1979-12-05
US4244943A (en)	1981-01-13
FR2425245B1 (de)	1983-03-11
GB2021412B (en)	1982-08-25
FR2425245A1 (fr)	1979-12-07
SE7904118L (sv)	1979-11-13
DE2917899A1 (de)	1979-11-22

Legal Events

Date	Code	Title	Description
1986-01-27	PHB	Application deemed withdrawn due to non-payment or other reasons

Publication	Publication Date	Title
US4244943A (en)	1981-01-13	Method for preparing urokinase injection
US5945098A (en)	1999-08-31	Stable intravenously-administrable immune globulin preparation
US5130244A (en)	1992-07-14	Stable aqueous thrombin solution
US7803911B2 (en)	2010-09-28	Dried blood factor composition comprising trehalose
US7381796B2 (en)	2008-06-03	Dried blood factor composition comprising trehalose
US4374763A (en)	1983-02-22	Method for producing gamma-globulin for use in intravenous administration and method for producing a pharmaceutical preparation thereof
WO1993001835A1 (fr)	1993-02-04	Preparation a anticorps monoclonal humain stabilise
IL117405A (en)	2002-05-23	Stable preparations of transglutaminase and processes for their preparation
AU738413B2 (en)	2001-09-20	Human growth hormone-containing aqueous pharmaceutical composition
JPS63165328A (ja)	1988-07-08	組織タンパクｐｐ４含有医薬
JPS6235756B2 (de)	1987-08-04
KR950010321B1 (ko)	1995-09-14	인간 트롬빈 제제의 가열처리방법
US4555401A (en)	1985-11-26	Live mumps vaccine and method of stabilizing the same
JPH0222233A (ja)	1990-01-25	スーパーオキシドディスムターゼ組成物
US2978385A (en)	1961-04-04	Stabilized chymotrypsin solution
US7244824B2 (en)	2007-07-17	Dried blood factor composition comprising trehalose
JP2003055257A (ja)	2003-02-26	安定な血液凝固第ｘｉｉｉ因子製剤
JPS6059000A (ja)	1985-04-05	インタ−フェロンの安定化方法
JP2722143B2 (ja)	1998-03-04	トリプシンインヒビター含有凍結乾燥製剤
JP2971680B2 (ja)	1999-11-08	組織プラスミノーゲン活性化因子含有組成物
SU1084024A1 (ru)	1984-04-07	Состав дл стабилизации стрептокиназы
JP2861655B2 (ja)	1999-02-24	ヒト尿性トリプシンインヒビター含有液状製剤及びその製造方法
EP0449897B1 (de)	1994-02-16	Ein reines faktor i-protein und verfahren zur herstellung
AU738891B2 (en)	2001-09-27	Stable transglutaminase preparations and process for producing them
JPS6115838A (ja)	1986-01-23	血液保存剤